Publication | Open Access
Major peptidoglycan transglycosylase activity in<i>Streptococcus pneumoniae</i>that is not a penicillin-binding protein
18
Citations
12
References
1985
Year
GlycobiologyBacteriologyEscherichia ColiPenicillin-binding ActivityPenicillin-binding ProteinsAntimicrobial ChemotherapyBacterial PathogensDrug ResistanceMedical MicrobiologyAntimicrobial ResistanceHealth SciencesAntimicrobial Drug DiscoveryBiochemistryMolecular MicrobiologyClinical MicrobiologyPenicillin-binding ProteinAntimicrobial SusceptibilityAntibioticsMicrobiologyMedicine
As in the Gram-positive cocci Staphylococcus aureus and Micrococcus luteus, which divide in 3 planes, Streptococcus pneumoniae, which divides on 1 fixed plane, possesses peptidoglycan transglycosylase activity that lacks penicillin-binding activity as the sole detectable transglycosylase activity in vitro. The penicillin-binding proteins (PBPs) in this organism did not show transglycosylase activity under the conditions in which the PBPs of Escherichia coli showed both transglycosylase and transpeptidase activities.
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